› 1fp7

X-ray diffraction
3.2Å resolution

MONOVALENT CATION BINDING SITES IN N10-FORMYLTETRAHYDROFOLATE SYNTHETASE FROM MOORELLA THERMOACETICA

Released:
DOI: 10.2210/pdb1fp7/pdb
PDB entry 1fp7 coloured by chain, front view.
PDB entry 1fp7 coloured by chain, side view.
PDB entry 1fp7 coloured by chain, top view.
Source organism: Moorella thermoacetica
Primary publication:
Cation binding and thermostability of FTHFS monovalent cation binding sites and thermostability of N10-formyltetrahydrofolate synthetase from Moorella thermoacetica.
Radfar R, Leaphart A, Brewer JM, Minor W, Odom JD, Dunlap RB, Lovell CR, Lebioda L
Biochemistry 39 14481-6 (2000)
PMID: 11087401

Function and Biology Details

Reaction catalysed: 
ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149118 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Formate--tetrahydrofolate ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 557 amino acids
Theoretical weight: 59.84 KDa
Source organism: Moorella thermoacetica
Expression system: Escherichia coli
UniProt:
  • Canonical: P21164 (Residues: 1-559; Coverage: 100%)
Gene name: fhs
Sequence domains: Formate--tetrahydrofolate ligase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand SO4 11 x SO4
Ligand K 1 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: R32
Unit cell:
a: 160.876Å b: 160.876Å c: 256.118Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.285 0.285 0.355
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Structural features of thermozymes.
Li et al. (2005)
9 other articles